Abstract
Abstract 1. 1. The blue carotenoprotein, linckiacyanin (λmax 395 and 612 nm), and a yellow carotenoprotein (λmax 403 nm) isolated from the skin of the starfish Linckia laevigata have been studied by resonance Raman and circular dichroism spectroscopy. 2. 2. Resonance Raman spectroscopy has provided evidence that the 400 and 600 nm absorption bands of linckiacyanin arise from two distinct types of carotenoid binding sites. 3. 3. Circular dichroism and resonance Raman spectral analysis support a chromophore exciton interaction mechanism as the origin of the 400 nm absorption band of linckiacyanin and yellow protein. 4. 4. Alterations in the absorption and circular dichroism spectra of linckiacyanin on heating suggest that the chromophore interaction responsible for the 400 nm absorption band is related to the quaternary helical structure of the protein.
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